|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
291-554 |
3.58e-45 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 160.91 E-value: 3.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 291 TFPFVARPVQSVVYTAAFGPILAAFVCAMVDSLLRGSRAARFQAIGYAPLALVGLVRLVTGVSPWLHSADAMVLFYFGCM 370
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 371 FEVLLTTLGVAERFVTIRRERDRVRNEADLlERLSETDPLTGLLNRRAIERQFEQL-----REVGFTALAVIDLDHFKAI 445
Cdd:COG2199 81 LELLLLLLALLLLLLALEDITELRRLEERL-RRLATHDPLTGLPNRRAFEERLERElararREGRPLALLLIDLDHFKRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 446 NDGYGHSTGDEVLKAVAVALKA--GSNVRAYRLGGEEFILLLRGQDVDaQAEFRRQAIPATVANA---VPGLAGPVTASM 520
Cdd:COG2199 160 NDTYGHAAGDEVLKEVARRLRAslRESDLVARLGGDEFAVLLPGTDLE-EAEALAERLREALEQLpfeLEGKELRVTVSI 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1109545722 521 GITAISSV-DAFTTVYERADKHLYEAKSAGRNRTR 554
Cdd:COG2199 239 GVALYPEDgDSAEELLRRADLALYRAKRAGRNRVV 273
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
407-554 |
3.99e-44 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 153.87 E-value: 3.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 407 TDPLTGLLNRRAIERQFEQL-----REVGFTALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKA--GSNVRAYRLGGE 479
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLlararRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSslRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109545722 480 EFILLLRGQDVDaQAEFRRQAIPATVANA--VPGLAGPVTASMGITAISS-VDAFTTVYERADKHLYEAKSAGRNRTR 554
Cdd:cd01949 82 EFAILLPGTDLE-EAEALAERLREAIEEPffIDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
403-553 |
2.63e-38 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 138.53 E-value: 2.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 403 RLSETDPLTGLLNRRAIERQFEQL-----REVGFTALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKagSNVR----A 473
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQElqraqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLS--SCLRpgdlL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 474 YRLGGEEFILLLRGQDVDaQAEFRRQAIPATVANAVP--GLAGPVTASMGITAIS-SVDAFTTVYERADKHLYEAKSAGR 550
Cdd:smart00267 79 ARLGGDEFALLLPETSLE-EAIALAERILQQLREPIIihGIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKKAGR 157
|
...
gi 1109545722 551 NRT 553
Cdd:smart00267 158 NQV 160
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
407-552 |
1.06e-37 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 136.61 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 407 TDPLTGLLNRRAIERQFEQL-----REVGFTALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKagSNVR----AYRLG 477
Cdd:pfam00990 3 HDPLTGLPNRRYFEEQLEQElqralREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLS--SSLRrsdlVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 478 GEEFILLLRGQDVD--------AQAEFRRQAIPATVAnavpGLAGPVTASMGItAISSVDAFT--TVYERADKHLYEAKS 547
Cdd:pfam00990 81 GDEFAILLPETSLEgaqelaerIRRLLAKLKIPHTVS----GLPLYVTISIGI-AAYPNDGEDpeDLLKRADTALYQAKQ 155
|
....*
gi 1109545722 548 AGRNR 552
Cdd:pfam00990 156 AGRNR 160
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
387-552 |
3.12e-33 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 132.33 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 387 IRRER--DRVRNEADLLERLSETDPLTGLLNRRAIERQFEQLREVGFT-----ALAVIDLDHFKAINDGYGHSTGDEVLK 459
Cdd:PRK09581 272 IRRKRyqDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERANErgkplSLMMIDIDHFKKVNDTYGHDAGDEVLR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 460 AVAVALKagSNVR----AYRLGGEEFILLLRGQDVD---AQAEFRRQAI---PATVANAVPGLagPVTASMGITAIS-SV 528
Cdd:PRK09581 352 EFAKRLR--NNIRgtdlIARYGGEEFVVVMPDTDIEdaiAVAERIRRKIaeePFIISDGKERL--NVTVSIGVAELRpSG 427
|
170 180
....*....|....*....|....
gi 1109545722 529 DAFTTVYERADKHLYEAKSAGRNR 552
Cdd:PRK09581 428 DTIEALIKRADKALYEAKNTGRNR 451
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
393-552 |
1.31e-32 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 125.48 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 393 RVRNEAdlLERLSETDPLTGLLNRRAI-ER---QFEQLREVGFT-ALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKA 467
Cdd:NF038266 84 RDLNEA--LREASTRDPLTGLPNRRLLmERlreEVERARRSGRPfTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 468 GsnVRAY----RLGGEEFILLL---RGQDVDAQAEFRRQAIpATVANAVPGLAGPVTASMGITAI-SSVDAFTTVYERAD 539
Cdd:NF038266 162 E--LREYdlcgRWGGEEFLLLLpetGLEEAQVVLERLREAV-RALAVRVGDDVLSVTASAGLAEHrPPEEGLSATLSRAD 238
|
170
....*....|...
gi 1109545722 540 KHLYEAKSAGRNR 552
Cdd:NF038266 239 QALYQAKRAGRDR 251
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
404-554 |
2.42e-32 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 122.06 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 404 LSETDPLTGLLNRRAIERQFEQLREVGFT-----ALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKagSNVR----AY 474
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRfqrsfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQ--SSVRgsdvVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 475 RLGGEEFILLLRG---QDVDAQAEFRRQAI---PATVANavpGLAGPVTASMGITAISS-VDAFTTVYERADKHLYEAKS 547
Cdd:TIGR00254 79 RYGGEEFVVILPGtplEDALSKAERLRDAInskPIEVAG---SETLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKK 155
|
....*..
gi 1109545722 548 AGRNRTR 554
Cdd:TIGR00254 156 AGRNRVV 162
|
|
| 7TMR-DISM_7TM |
pfam07695 |
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ... |
179-383 |
1.91e-13 |
|
7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).
Pssm-ID: 429600 [Multi-domain] Cd Length: 207 Bit Score: 69.61 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 179 LLIAGLAGMLVMPLIFNAAFYRALREPFVLWHSVLTTSLLMTIVVTSGLSVALFDPPAMTLSW---MTTLLFGVTISSGA 255
Cdd:pfam07695 3 LLLGLFYGILLALALYNLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNAPPWLNnklLYLSLLLLLPFFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 256 MFTYSFIEPGMMHPLLRRILPYCAAWAVFLSVFHATFPFVarPVQSVVYTAAFGPILAAFVCAMVdSLLRGSRAARFQAI 335
Cdd:pfam07695 83 LFARSFLELKKYLPRLLRLLLGLALLLALLLLLLPLFPYT--LSLPLAQLLALLFILFLLLLGII-AWRKGYKPARYFLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1109545722 336 GYAPLALVGLVRLVTGVSPWLHSADAMVLFYFGCMFEVLLTTLGVAER 383
Cdd:pfam07695 160 AWLLLLIGALIDILSLLGLLPSNFFTNYLLQIGSALEVLLLSLALADR 207
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
291-554 |
3.58e-45 |
|
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];
Pssm-ID: 441801 [Multi-domain] Cd Length: 275 Bit Score: 160.91 E-value: 3.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 291 TFPFVARPVQSVVYTAAFGPILAAFVCAMVDSLLRGSRAARFQAIGYAPLALVGLVRLVTGVSPWLHSADAMVLFYFGCM 370
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 371 FEVLLTTLGVAERFVTIRRERDRVRNEADLlERLSETDPLTGLLNRRAIERQFEQL-----REVGFTALAVIDLDHFKAI 445
Cdd:COG2199 81 LELLLLLLALLLLLLALEDITELRRLEERL-RRLATHDPLTGLPNRRAFEERLERElararREGRPLALLLIDLDHFKRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 446 NDGYGHSTGDEVLKAVAVALKA--GSNVRAYRLGGEEFILLLRGQDVDaQAEFRRQAIPATVANA---VPGLAGPVTASM 520
Cdd:COG2199 160 NDTYGHAAGDEVLKEVARRLRAslRESDLVARLGGDEFAVLLPGTDLE-EAEALAERLREALEQLpfeLEGKELRVTVSI 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1109545722 521 GITAISSV-DAFTTVYERADKHLYEAKSAGRNRTR 554
Cdd:COG2199 239 GVALYPEDgDSAEELLRRADLALYRAKRAGRNRVV 273
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
407-554 |
3.99e-44 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 153.87 E-value: 3.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 407 TDPLTGLLNRRAIERQFEQL-----REVGFTALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKA--GSNVRAYRLGGE 479
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLlararRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSslRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109545722 480 EFILLLRGQDVDaQAEFRRQAIPATVANA--VPGLAGPVTASMGITAISS-VDAFTTVYERADKHLYEAKSAGRNRTR 554
Cdd:cd01949 82 EFAILLPGTDLE-EAEALAERLREAIEEPffIDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
403-553 |
2.63e-38 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 138.53 E-value: 2.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 403 RLSETDPLTGLLNRRAIERQFEQL-----REVGFTALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKagSNVR----A 473
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQElqraqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLS--SCLRpgdlL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 474 YRLGGEEFILLLRGQDVDaQAEFRRQAIPATVANAVP--GLAGPVTASMGITAIS-SVDAFTTVYERADKHLYEAKSAGR 550
Cdd:smart00267 79 ARLGGDEFALLLPETSLE-EAIALAERILQQLREPIIihGIPLYLTISIGVAAYPnPGEDAEDLLKRADTALYQAKKAGR 157
|
...
gi 1109545722 551 NRT 553
Cdd:smart00267 158 NQV 160
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
407-552 |
1.06e-37 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 136.61 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 407 TDPLTGLLNRRAIERQFEQL-----REVGFTALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKagSNVR----AYRLG 477
Cdd:pfam00990 3 HDPLTGLPNRRYFEEQLEQElqralREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLS--SSLRrsdlVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 478 GEEFILLLRGQDVD--------AQAEFRRQAIPATVAnavpGLAGPVTASMGItAISSVDAFT--TVYERADKHLYEAKS 547
Cdd:pfam00990 81 GDEFAILLPETSLEgaqelaerIRRLLAKLKIPHTVS----GLPLYVTISIGI-AAYPNDGEDpeDLLKRADTALYQAKQ 155
|
....*
gi 1109545722 548 AGRNR 552
Cdd:pfam00990 156 AGRNR 160
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
387-552 |
3.12e-33 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 132.33 E-value: 3.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 387 IRRER--DRVRNEADLLERLSETDPLTGLLNRRAIERQFEQLREVGFT-----ALAVIDLDHFKAINDGYGHSTGDEVLK 459
Cdd:PRK09581 272 IRRKRyqDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERANErgkplSLMMIDIDHFKKVNDTYGHDAGDEVLR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 460 AVAVALKagSNVR----AYRLGGEEFILLLRGQDVD---AQAEFRRQAI---PATVANAVPGLagPVTASMGITAIS-SV 528
Cdd:PRK09581 352 EFAKRLR--NNIRgtdlIARYGGEEFVVVMPDTDIEdaiAVAERIRRKIaeePFIISDGKERL--NVTVSIGVAELRpSG 427
|
170 180
....*....|....*....|....
gi 1109545722 529 DAFTTVYERADKHLYEAKSAGRNR 552
Cdd:PRK09581 428 DTIEALIKRADKALYEAKNTGRNR 451
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
393-552 |
1.31e-32 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 125.48 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 393 RVRNEAdlLERLSETDPLTGLLNRRAI-ER---QFEQLREVGFT-ALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKA 467
Cdd:NF038266 84 RDLNEA--LREASTRDPLTGLPNRRLLmERlreEVERARRSGRPfTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 468 GsnVRAY----RLGGEEFILLL---RGQDVDAQAEFRRQAIpATVANAVPGLAGPVTASMGITAI-SSVDAFTTVYERAD 539
Cdd:NF038266 162 E--LREYdlcgRWGGEEFLLLLpetGLEEAQVVLERLREAV-RALAVRVGDDVLSVTASAGLAEHrPPEEGLSATLSRAD 238
|
170
....*....|...
gi 1109545722 540 KHLYEAKSAGRNR 552
Cdd:NF038266 239 QALYQAKRAGRDR 251
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
170-554 |
1.87e-32 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 132.59 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 170 ASAADLRFLLLIAGLAGMLVMPLIFNAAFYRALREPFVLWHSVLTTSLLMTIVVTSGLSVALFDPPAMTLSWMTTLLFGV 249
Cdd:COG5001 19 LLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 250 TISSGAMFTYSFIEPGMMHPLLRRILPYCAAWAVFLSVFHATFPFVARPVQSVVYTAAFGPILAAFVCAMVDSLLRGSRA 329
Cdd:COG5001 99 LLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 330 ARFQAIGYAPLALVGLVRLVTGVSPWLHSADAMVLFYFGCMFEVLLTTLGVAERFVTIRRERDRVRNEadlLERLSETDP 409
Cdd:COG5001 179 LLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEER---LRHLAYHDP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 410 LTGLLNRRAIERQFEQL-----REVGFTALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKA--GSNVRAYRLGGEEFI 482
Cdd:COG5001 256 LTGLPNRRLFLDRLEQAlararRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRAclREGDTVARLGGDEFA 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109545722 483 LLLRGQDVDAQAEFRRQAIPATVANAVPgLAG---PVTASMGItAISSVDA--FTTVYERADKHLYEAKSAGRNRTR 554
Cdd:COG5001 336 VLLPDLDDPEDAEAVAERILAALAEPFE-LDGhelYVSASIGI-ALYPDDGadAEELLRNADLAMYRAKAAGRNRYR 410
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
404-554 |
2.42e-32 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 122.06 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 404 LSETDPLTGLLNRRAIERQFEQLREVGFT-----ALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKagSNVR----AY 474
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRfqrsfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQ--SSVRgsdvVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 475 RLGGEEFILLLRG---QDVDAQAEFRRQAI---PATVANavpGLAGPVTASMGITAISS-VDAFTTVYERADKHLYEAKS 547
Cdd:TIGR00254 79 RYGGEEFVVILPGtplEDALSKAERLRDAInskPIEVAG---SETLTVTVSIGVACYPGhGLTLEELLKRADEALYQAKK 155
|
....*..
gi 1109545722 548 AGRNRTR 554
Cdd:TIGR00254 156 AGRNRVV 162
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
379-553 |
1.03e-31 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 124.41 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 379 GVAERFVTIRRERDRVrnEADLLERLSETDPLTGLLNRR----AIERQFEQLREVGFtALAVIDLDHFKAINDGYGHSTG 454
Cdd:PRK09894 105 AFQEGLLSFTAALTDY--KIYLLTIRSNMDVLTGLPGRRvldeSFDHQLRNREPQNL-YLALLDIDRFKLVNDTYGHLIG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 455 DEVLKAVAVALKAG--SNVRAYRLGGEEFILLLRGQ-DVDAQ--AEFRRQAIpATVANAVPGLAGPVTASMGITAISSVD 529
Cdd:PRK09894 182 DVVLRTLATYLASWtrDYETVYRYGGEEFIICLKAAtDEEACraGERIRQLI-ANHAITHSDGRINITATFGVSRAFPEE 260
|
170 180
....*....|....*....|....
gi 1109545722 530 AFTTVYERADKHLYEAKSAGRNRT 553
Cdd:PRK09894 261 TLDVVIGRADRAMYEGKQTGRNRV 284
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
326-552 |
1.54e-25 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 110.87 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 326 GSRAARFQAIGYAPLALVGLVRLVTGVSPWLHS---ADAMVLFYFGCMfevLLTTLGVaerfvtIRRerdRVRNEADL-- 400
Cdd:PRK15426 325 GSRYVSWERLDHFDGVLVRVHTLREGVRGDFGSisiALTLLWALFTAM---LLISWYV------IRR---MVSNMFVLqs 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 401 -LERLSETDPLTGLLNRRAIERQFEQLREVGFTA---LAVI--DLDHFKAINDGYGHSTGDEVLKAVAVALkaGSNVRAY 474
Cdd:PRK15426 393 sLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDqqpFSVIqlDLDHFKSINDRFGHQAGDRVLSHAAGLI--SSSLRAQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 475 ----RLGGEEFILLLRG---QDVDAQAEFRRQAIPATVANAVPGLAGPVTASMGITAIS-----SVDAFTTVyerADKHL 542
Cdd:PRK15426 471 dvagRVGGEEFCVVLPGaslAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSSAEedgdyDFEQLQSL---ADRRL 547
|
250
....*....|
gi 1109545722 543 YEAKSAGRNR 552
Cdd:PRK15426 548 YLAKQAGRNR 557
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
408-552 |
4.89e-18 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 88.19 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 408 DPLTGLLNRRAIERQFEQL----REVGF-TALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKA---GSNVRAyRLGGE 479
Cdd:PRK09776 668 DALTHLANRASFEKQLRRLlqtvNSTHQrHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSmlrSSDVLA-RLGGD 746
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109545722 480 EFILLLRGQDVDaQAEFRRQAIPATVaNAVP----GLAGPVTASMGITAI-SSVDAFTTVYERADKHLYEAKSAGRNR 552
Cdd:PRK09776 747 EFGLLLPDCNVE-SARFIATRIISAI-NDYHfpweGRVYRVGASAGITLIdANNHQASEVMSQADIACYAAKNAGRGR 822
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
391-546 |
1.95e-15 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 78.51 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 391 RDRVRNeADLLeRLSETDPLTGLLNRRAIERQFEQLRE----VGFTALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALK 466
Cdd:PRK09966 236 RLQAKN-AQLL-RTALHDPLTGLANRAAFRSGINTLMNnsdaRKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 467 --AGSNVRAYRLGGEEFILLLrgqdVDAQAEFRRQAIPATVANAVP-------GLAGPVTASMGITAISSVDAFTTVYER 537
Cdd:PRK09966 314 efGGLRHKAYRLGGDEFAMVL----YDVQSESEVQQICSALTQIFNlpfdlhnGHQTTMTLSIGYAMTIEHASAEKLQEL 389
|
....*....
gi 1109545722 538 ADKHLYEAK 546
Cdd:PRK09966 390 ADHNMYQAK 398
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
395-484 |
3.24e-15 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 78.96 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 395 RNEADLLERLSETDPLTGLLNRRAI-ERQFEQLREVGFTALAVI--DLDHFKAINDGYGHSTGDEVLKAVAVALKA--GS 469
Cdd:PRK10060 227 RRAQERLRILANTDSITGLPNRNAIqELIDHAINAADNNQVGIVylDLDNFKKVNDAYGHMFGDQLLQDVSLAILSclEE 306
|
90
....*....|....*
gi 1109545722 470 NVRAYRLGGEEFILL 484
Cdd:PRK10060 307 DQTLARLGGDEFLVL 321
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
401-553 |
9.76e-14 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 72.94 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 401 LERLSETDPLTGLLNRRAIE----RQFEQ-LREVGFTALAVIDLDHFKAINDGYGHSTGDEVLKAVAVALKA---GSNVR 472
Cdd:PRK10245 201 LQVMSTRDGMTGVYNRRHWEtllrNEFDNcRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQItlrGSDVI 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 473 AyRLGGEEFILLLRGQDVDAQ-----------AEFRRQAIPATVANAVPGLAgPVTASMGitaissvdAFTTVYERADKH 541
Cdd:PRK10245 281 G-RFGGDEFAVIMSGTPAESAitamsrvheglNTLRLPNAPQVTLRISVGVA-PLNPQMS--------HYREWLKSADLA 350
|
170
....*....|..
gi 1109545722 542 LYEAKSAGRNRT 553
Cdd:PRK10245 351 LYKAKNAGRNRT 362
|
|
| 7TMR-DISM_7TM |
pfam07695 |
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ... |
179-383 |
1.91e-13 |
|
7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).
Pssm-ID: 429600 [Multi-domain] Cd Length: 207 Bit Score: 69.61 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 179 LLIAGLAGMLVMPLIFNAAFYRALREPFVLWHSVLTTSLLMTIVVTSGLSVALFDPPAMTLSW---MTTLLFGVTISSGA 255
Cdd:pfam07695 3 LLLGLFYGILLALALYNLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNAPPWLNnklLYLSLLLLLPFFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 256 MFTYSFIEPGMMHPLLRRILPYCAAWAVFLSVFHATFPFVarPVQSVVYTAAFGPILAAFVCAMVdSLLRGSRAARFQAI 335
Cdd:pfam07695 83 LFARSFLELKKYLPRLLRLLLGLALLLALLLLLLPLFPYT--LSLPLAQLLALLFILFLLLLGII-AWRKGYKPARYFLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1109545722 336 GYAPLALVGLVRLVTGVSPWLHSADAMVLFYFGCMFEVLLTTLGVAER 383
Cdd:pfam07695 160 AWLLLLIGALIDILSLLGLLPSNFFTNYLLQIGSALEVLLLSLALADR 207
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
387-523 |
2.51e-10 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 63.25 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 387 IRRERDRVRneadlLERLSETDPLTGLLNRRAIERQFEQL----REVgftALAVIDLDHFKAINDGYGHSTGDEVLKAVA 462
Cdd:PRK11359 363 LEQEKSRQH-----IEQLIQFDPLTGLPNRNNLHNYLDDLvdkaVSP---VVYLIGVDHFQDVIDSLGYAWADQALLEVV 434
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109545722 463 VALKAGSNVRAY--RLGGEEFILLLRGQDVDAQAEFRRQAIpaTVANAVPGLAG---PVTASMGIT 523
Cdd:PRK11359 435 NRFREKLKPDQYlcRIEGTQFVLVSLENDVSNITQIADELR--NVVSKPIMIDDkpfPLTLSIGIS 498
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
473-546 |
2.08e-04 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 42.20 E-value: 2.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109545722 473 AYRLGGEEFILLLRGQDVDaQAEFRRQAIPATVANAVPglaGPVTASMGItaissvdAFTTVYERADKhLYEAK 546
Cdd:COG3706 118 VARYGGEEFAILLPGTDLE-GALAVAERIREAVAELPS---LRVTVSIGV-------AGDSLLKRADA-LYQAR 179
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
437-522 |
4.80e-03 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 37.72 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109545722 437 IDLDHFKAINDGYGHSTGDEVLKAVAVALKAG---SNVRAYRLGGEEFILLLRGQDVDAQAEFRRQAIPAtVANAVPGLA 513
Cdd:cd07556 7 ADIVGFTSLADALGPDEGDELLNELAGRFDSLirrSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREA-VSALNQSEG 85
|
....*....
gi 1109545722 514 GPVTASMGI 522
Cdd:cd07556 86 NPVRVRIGI 94
|
|
| |
